PDBsum entry 2f8v

Contractile protein/contractile protein

PDB id: 2f8v

Contents

Protein chains

194 a.a. *

88 a.a. *

Ligands

SO4 ×5

Waters ×79

* Residue conservation analysis

PDB id:

2f8v

Name:

Contractile protein/contractile protein

Title:

Structure of full length telethonin in complex with the n-terminus of titin

Structure:

N2b-titin isoform. Chain: a, b, c, d. Fragment: domains z1z2, residues 1-196. Engineered: yes. Telethonin. Chain: t, y. Synonym: titin cap protein. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: tcap. Expression_system_taxid: 562

Biol. unit:

Trimer (from PQS)

Resolution:

2.75Å R-factor: 0.267 R-free: 0.287

Authors:

N.Pinotsis,M.Petoukhov,S.Lange,D.Svergun,P.Zou,M.Gautel,M.Wilmanns

Key ref:

N.Pinotsis et al. (2006). Evidence for a dimeric assembly of two titin/telethonin complexes induced by the telethonin C-terminus. J Struct Biol, 155, 239-250. PubMed id: 16713295 DOI: 10.1016/j.jsb.2006.03.028

Date:

04-Dec-05 Release date: 27-Jun-06

Protein chains

Q8WZ42  (TITIN_HUMAN) -  Titin from Homo sapiens

Seq: 34350 a.a.

Struc: 194 a.a.

Protein chains

O15273  (TELT_HUMAN) -  Telethonin from Homo sapiens

Seq: 167 a.a.

Struc: 88 a.a.*

* PDB and UniProt seqs differ at 4 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chains A, B, C, D: E.C.2.7.11.1 - non-specific serine/threonine protein kinase.
• Reaction:
  1. L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H⁺
  2. L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H⁺

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1016/j.jsb.2006.03.028

J Struct Biol 155:239-250 (2006)

PubMed id: 16713295

Evidence for a dimeric assembly of two titin/telethonin complexes induced by the telethonin C-terminus.

N.Pinotsis, M.Petoukhov, S.Lange, D.Svergun, P.Zou, M.Gautel, M.Wilmanns.

ABSTRACT

The Z-disk region defines the lateral boundary of the sarcomere and requires a high level of mechanical strength to provide a stable framework for large filamentous muscle proteins. The level of complexity at this area is reflected by a large number of protein-protein interactions. Recently, we unraveled how the N-terminus of the longest filament component, the giant muscle protein titin, is assembled into an antiparallel (2:1) sandwich complex by the N-terminal titin-binding segment of the Z-disk ligand telethonin/T-cap [Zou, P., Pinotsis, N., Lange, S., Song, Y.H., Popov, A., Mavridis, I., Mayans, O.M., Gautel, M., Wilmanns, M., 2006. Palindromic assembly of the giant muscle protein titin in the sarcomeric Z-disk. Nature 439, 229-233]. In this contribution, we present structural data of a related complex of the titin N-terminus with full-length telethonin. The C-terminus of telethonin remains invisible, suggesting that it does not fold into a defined structure even in the presence of titin. In contrast to the structure with truncated telethonin, a dimer of two titin/telethonin complexes is formed within the crystal environment, potentially indicating the formation of higher oligomers. We further investigated the structure and dynamics of this assembly by small-angle X-ray scattering, circular dichroism, and in vivo complementation data. The data consistently indicate the involvement of the C-terminal part of telethonin into the assembly of two titin/telethonin complexes.